pubmed-article:14592421 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14592421 | lifeskim:mentions | umls-concept:C0919490 | lld:lifeskim |
pubmed-article:14592421 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:14592421 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:14592421 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
pubmed-article:14592421 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:14592421 | lifeskim:mentions | umls-concept:C0687760 | lld:lifeskim |
pubmed-article:14592421 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:14592421 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:14592421 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:14592421 | pubmed:dateCreated | 2003-10-31 | lld:pubmed |
pubmed-article:14592421 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:abstractText | PU.1 is a member of the Ets family of transcription factors and plays critical roles in the development of hematopoietic cells such as macrophages and B cells. To elucidate the molecular mechanism(s) underlying the regulation of PU.1 function, we screened for PU.1 interacting proteins using a yeast two-hybrid approach. As a result, a novel PU.1 binding factor, which we termed Pub, was isolated. The Pub protein has one B-box zinc finger domain, followed by a coiled-coil region and a B30.2-like domain, these features being characteristic of the tripartite motif (TRIM) family of protein. The PEST domain of PU.1 was found to interact with the N-terminal portion of Pub, a region that includes the TRIM which is considered to mediate protein-protein interactions. Northern blot and RT-PCR analyses demonstrated that Pub is predominantly expressed in hematopoietic tissues and cells where PU.1 is also expressed. Using a luciferase-based assay, we showed that Pub inhibited the transcriptional activity of PU.1. Moreover, the B-box zinc finger domain of Pub was critical for this inhibitory activity. These data suggest that Pub may be important in regulating the transcriptional activity of PU.1. | lld:pubmed |
pubmed-article:14592421 | pubmed:language | eng | lld:pubmed |
pubmed-article:14592421 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14592421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14592421 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14592421 | pubmed:month | Nov | lld:pubmed |
pubmed-article:14592421 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:14592421 | pubmed:author | pubmed-author:HiroseSatoshi... | lld:pubmed |
pubmed-article:14592421 | pubmed:author | pubmed-author:NishizumiHiro... | lld:pubmed |
pubmed-article:14592421 | pubmed:author | pubmed-author:SakanoHitoshi... | lld:pubmed |
pubmed-article:14592421 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14592421 | pubmed:day | 14 | lld:pubmed |
pubmed-article:14592421 | pubmed:volume | 311 | lld:pubmed |
pubmed-article:14592421 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14592421 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14592421 | pubmed:pagination | 351-60 | lld:pubmed |
pubmed-article:14592421 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:meshHeading | pubmed-meshheading:14592421... | lld:pubmed |
pubmed-article:14592421 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14592421 | pubmed:articleTitle | Pub, a novel PU.1 binding protein, regulates the transcriptional activity of PU.1. | lld:pubmed |
pubmed-article:14592421 | pubmed:affiliation | Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. | lld:pubmed |
pubmed-article:14592421 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14592421 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:74735 | entrezgene:pubmed | pubmed-article:14592421 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14592421 | lld:pubmed |